Results 121 to 130 of about 1,094 (157)

Tracking of Prosaposin, a Saposin Precursor, in Rat Testis [PDF]

open access: yesJournal of Histochemistry & Cytochemistry, 2023
We tracked prosaposin (PSAP), a trophic factor, using an antibody specific to its proteolytic portion and an antibody to sortilin that traffics PSAP only to the lysosome. Immunostaining revealed that PSAP was distributed mainly on the basal side of seminiferous tubules, where many Sertoli cells and pachytene spermatocytes contained PSAP and its ...
Kimiko Yamamiya   +8 more
openaire   +3 more sources

Characterization of Human Saposins by NMR Spectroscopy†

Biochemistry, 2006
Saposins are lipid-binding and membrane-perturbing glycoproteins of the mammalian lysosomes involved in sphingolipid and membrane digestion. Although the four human saposins (Saps), A-D, are sequence-related, they are responsible for the activation of different steps in the cascade of lysosomal glycosphingolipid degradation. Saposin activity is maximal
Michael John   +2 more
exaly   +3 more sources

Saposins (sap) A and C activate the degradation of galactosylceramide in living cells [PDF]

open access: yesFEBS Letters, 1997
In loading tests using galactosylceramide which had been labelled with tritium in the ceramide moiety, living skin fibroblast lines derived from the original prosaposin-deficient patients had a markedly reduced capacity to degrade galactosylceramide. The
Thierry Levade   +2 more
exaly   +2 more sources

Saposins A, B, C, and D in Plasma of Patients with Lysosomal Storage Disorders

open access: yesClinical Chemistry, 2000
BackgroundEarly diagnosis of lysosomal storage disorders (LSDs), before the onset of irreversible pathology, will be critical for maximum efficacy of many current and proposed therapies. To search for potential markers of LSDs, we measured saposins A, B,
Peter Meikle   +2 more
exaly   +2 more sources

Lysosomal Proteolysis of Prosaposin, the Precursor of Saposins (Sphingolipid Activator Proteins): Its Mechanism and Inhibition by Ganglioside

open access: yesArchives of Biochemistry and Biophysics, 1997
Saposins A, B, C, and D, which are required for the enzymatic hydrolysis of sphingolipids by specific lysosomal hydrolases, are produced by proteolytic processing of their common precursor protein, prosaposin.
Shoji Tsuji   +2 more
exaly   +2 more sources

Crystal Structures of Human Saposins C and D: Implications for Lipid Recognition and Membrane Interactions [PDF]

open access: yesStructure, 2008
SummaryHuman saposins are essential proteins required for degradation of sphingolipids and lipid antigen presentation. Despite the conserved structural organization of saposins, their distinct modes of interaction with biological membranes are not fully ...
Maxim Rossmann   +2 more
exaly   +2 more sources

Combined saposin deficiency: A rare occurrence

Medical Journal Armed Forces India, 2023
Combined saposin deficiency (OMIM #611721), an exceedingly rare lysosomal storage disorder, is caused by a mutation in the gene PSAP. This gene encodes a protein, prosaposin, that cleaves into four constituent proteins, each of which has a role as a cofactor for the enzymes whose deficiency results in Krabbe disease, metachromatic leukodystrophy ...
Vivek Bhat   +3 more
openaire   +2 more sources

Saposins and Their Interaction with Lipids

Neurochemical Research, 1999
The lysosomal degradation of several sphingolipids requires the presence of four small glycoproteins called saposins, generated by proteolytic processing of a common precursor, prosaposin. Saposins share several structural properties, including six similarly located cysteines forming three disulfide bridges with the same cysteine pairings.
A M, Vaccaro   +3 more
openaire   +2 more sources

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